The architecture of the binding site in redox protein complexes: implications for fast dissociation.

Crowley, Peter B; Carrondo, Maria Arménia

Crowley, Peter B; Carrondo, Maria Arménia.

Afiliación

Crowley PB; Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. Da República, Apartado 127, 2781 901 Oeiras, Portugal. crowley@itqb.unl.pt

Proteins ; 55(3): 603-12, 2004 May 15.

Article en En | MEDLINE | ID: mdl-15103624

RESUMEN

Interprotein electron transfer is characterized by protein interactions on the millisecond time scale. Such transient encounters are ensured by extremely high rates of complex dissociation. Computational analysis of the available crystal structures of redox protein complexes reveals features of the binding site that favor fast dissociation. In particular, the complex interface is shown to have low geometric complementarity and poor packing. These features are consistent with the necessity for fast dissociation since the absence of close packing facilitates solvation of the interface and disruption of the complex.

Asunto(s)

Proteínas/química; Aminoácidos/química; Sitios de Unión; Transporte de Electrón; Cinética; Sustancias Macromoleculares; Modelos Moleculares; Estructura Molecular; Oxidación-Reducción; Conformación Proteica; Proteínas/metabolismo; Electricidad Estática

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Idioma: En Revista: Proteins Asunto de la revista: BIOQUIMICA Año: 2004 Tipo del documento: Article País de afiliación: Portugal Pais de publicación: Estados Unidos

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